Ankyrin repeat and SAM domain-containing protein 1A (ANKS1A)
The protein contains 1134 amino acids for an estimated molecular weight of 123108 Da.
Regulator of different signaling pathways. Regulates EPHA8 receptor tyrosine kinase signaling to control cell migration and neurite retraction (By similarity). (updated: Oct. 10, 2018)
Protein identification was indicated in the following studies:
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| dbSNP:rs6930932 | |
| dbSNP:rs820085 |
The reference OMIM entry for this protein is 608994
Ankyrin repeat and sterile alpha motif domains-containing protein 1a; anks1a
Odin
Kiaa0229
CLONING
By sequencing clones obtained from a size-fractionated immature myeloid cell line (KG-1) cDNA library, Nagase et al. (1996) cloned ANKS1, which they designated KIAA0229. The deduced 1,180-amino acid protein shares 21.7% identity with ankyrin-1 (ANK1; 612641) over 652 amino acids. Northern blot analysis detected ANKS1 expression in all tissues examined, with highest expression in heart, skeletal muscle, and pancreas. KG-1 and HeLa cell lines also showed high ANKS1 expression. Using a proteomic approach, Pandey et al. (2002) identified ANKS1, which they named Odin after a deity in Nordic mythology, as a protein tyrosine phosphorylated following growth factor stimulation of HeLa cells. By peptide sequence analysis, they identified the Odin cDNA. The deduced 1,134-amino acid protein has a calculated molecular mass of about 123 kD. It has 6 N-terminal tandem ankyrin repeats, followed by 2 sterile alpha motif (SAM) domains and a C-terminal phosphotyrosine-binding (PTB) domain. Northern blot analysis detected a 6.0-kb transcript in nearly all tissues and cell lines tested. Western blot analysis of mouse tissues and human and rodent cell lines detected Odin expressed at an apparent molecular mass of 130 kD. Immunofluorescence and Western blot analysis found Odin was expressed as a cytoplasmic protein.GENE FUNCTION
Pandey et al. (2002) found that Odin was tyrosine phosphorylated upon addition of growth factors, such as EGF (131530) or PDGF (see 190040), but not by cytokines, such as IL3 (147740) or erythropoietin (133170). The PTB domain was not required for its tyrosine phosphorylation. Overexpression of Odin inhibited EGF-induced activation of the FOS (164810) promoter, and microinjection of either wildtype or mutant Odin lacking the PTB domain inhibited PDGF-induced mitogenesis in mouse fibroblasts. Pandey et al. (2002) concluded that Odin plays a negative role in growth factor receptor signaling pathways.GENE STRUCTURE
The ANKS1A gene contains 24 exons and spans about 200 kb (Kristiansen et al., 2004).MAPPING
By radiation hybrid and somatic cell hybrid analyses, Nagase et al. (1996) mapped the ANKS1A gene to chromosome 6.ANIMAL MODEL
Kristiansen et al. (2004) generated Odin-deficient mice by gene targeting. Mutant mice were indistinguishable from wildtype controls, and histologic examination of the kidney, lung, and liver showed no major abnormalities. However, embryonic fibroblasts from Odin-deficient mice exhibited a hyperproliferative phenotype compared with wildtype embryonic fibroblasts, consistent with a role for Odin as a negative regulator of growth factor receptor signaling. ... More on the omim web site
June 29, 2020: Protein entry updated
Automatic update: OMIM entry 608994 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).